Publication: Characterization of recombinant Beta vulgaris 4,5-DOPA-extradiol-dioxygenase active in the biosynthesis of betalains
Authors
Gandía Herrero, Fernando ; García Carmona, Francisco
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Publisher
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DOI
https://doi.org/10.1007/s00425-012-1593-2
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info:eu-repo/semantics/article
Description
© Springer-Verlag 2012.
This document is the Published version of a Published Work that
appeared in final form in Planta. To access the final edited and published work see https://doi.org/10.1007/s00425-012-1593-2
Abstract
Betalains are water-soluble pigments with high antiradical capacity which bestow bright colors to flowers,
fruits and other parts of most plants of the order Caryophyllales. The formation of the structural unit of all betalains, betalamic acid from the precursor amino acid 4,5-dihydroxyphenylalanine is catalyzed by the enzyme 4,5-DOPAextradiol-dioxygenase followed by intramolecular cyclization of the 4,5-secodopa intermediate. This paper describes the purification and the molecular and functional characterization of an active 4,5-DOPA-extradiol-dioxygenase from the best-known source of betalains—Beta vulgaris—after heterologous expression in Escherichia coli. The enzyme is a monomeric protein with a molecular mass of 32 kDa characterized by chromatography, electrophoresis and MALDITOF analysis. Enzyme kinetic properties are characterized in
the production of betalamic acid, the structural, chromophoric and bioactive unit of plant pigment betalains.
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Citation
Planta (2012) 236:91–100. 2012 Vol. 236 Nº 1 Pág.: 91-100
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